Thrombin-induced inhibition of myoblast differentiation is mediated by Gβγ

被引:9
|
作者
Nagao, M [1 ]
Kaziro, Y [1 ]
Itoh, H [1 ]
机构
[1] Tokyo Inst Technol, Fac Biosci & Biotechnol, Midori Ku, Yokohama, Kanagawa 2268501, Japan
基金
日本学术振兴会;
关键词
thrombin; G protein; G beta gamma; myoblast differentiation; G alpha(12); myotube formation;
D O I
10.1016/S0014-5793(00)01458-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Thrombin has been shown to inhibit skeletal muscle differentiation, However, the mechanisms by which thrombin represses myogenesis remain unknown. Since the thrombin receptor couples to G(i), G(q/11) and G(12), we examined which subunits of heterotrimeric guanine nucleotide-binding regulatory proteins (G alpha(i), G alpha(q/11), G alpha(12) or G beta gamma) participate in the thrombin-induced inhibition of C2C12 myoblast differentiation. G alpha(i2) and G alpha(11) had no inhibitory effect on the myogenic differentiation, G alpha(12) prevented only myoblast fusion, whereas G beta gamma inhibit ed both the induction of skeletal muscle-specific markers and the myotube formation. In addition, the thrombin-induced reduction of creatine kinase activity was blocked by the C-terminal peptide of beta-adrenergic receptor kinase, which is known to sequester free G beta gamma, These results suggest that the thrombin-induced inhibition of muscle differentiation is mainly mediated by G beta gamma. (C) 2000 Federation of European Biochemical Societies.
引用
收藏
页码:297 / 301
页数:5
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